Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot P59510 (ATS20_HUMAN)

Last modified July 22, 2008. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    ADAMTS-20
    EC=3.4.24.-
Alternative name(s):
    A disintegrin and metalloproteinase with thrombospondin motifs 20
      Short name(s)=ADAM-TS 20, ADAM-TS20
Gene names
Name: ADAMTS20
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1911 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

May play a role in tissue-remodeling process occurring in both normal and pathological conditions.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrixBy similarity.

Tissue specificity

Very sparingly expressed, although is detected at low levels in testis, prostate, ovary, heart, placenta, lung and pancreas. Overexpressed in several brain, colon and breast carcinomas.

Post-translational modification

The precursor is cleaved by a furin endopeptidase By similarity.

Sequence similarities

Contains 1 disintegrin domain.

Contains 1 GON domain.

Contains 1 peptidase M12B domain.

Contains 15 TSP type-1 domains.

Ontologies

Keywords

   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMCleavage on pair of basic residues
Glycoprotein
Zymogen

Gene Ontology (GO)

None. [Check GOA]

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P59510-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P59510-2)

The sequence of this isoform differs from the canonical sequence as follows:
     683-693: THDICVQGQCM → SYNIDCNCVLK
     1430-1504: CSASCGKGRK...QQRDVYCRLK → EDLKVKLLPQ...GDLKYYKNSL
     1505-1911: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 253232 By similarity
Chain254 – 19111658ADAMTS-20

Regions

Domain259 – 467209Peptidase M12B
Domain468 – 55588Disintegrin
Domain556 – 61156TSP type-1 1
Domain847 – 90559TSP type-1 2
Domain906 – 96257TSP type-1 3
Domain967 – 102458TSP type-1 4
Domain1025 – 107450TSP type-1 5
Domain1077 – 113660TSP type-1 6
Domain1153 – 120755TSP type-1 7
Domain1208 – 126558TSP type-1 8
Domain1305 – 135753TSP type-1 9
Domain1359 – 141759TSP type-1 10
Domain1418 – 147659TSP type-1 11
Domain1477 – 153256TSP type-1 12
Domain1536 – 158954TSP type-1 13
Domain1590 – 165364TSP type-1 14
Domain1655 – 171157TSP type-1 15
Domain1712 – 1911200GON
Region724 – 846123Spacer
Compositional bias612 – 723112Cys-rich

Sites

Active site4041 By similarity
Metal binding4031Zinc (catalytic) By similarity
Metal binding4071Zinc (catalytic) By similarity
Metal binding4131Zinc (catalytic) By similarity

Amino acid modifications

Glycosylation921N-linked (GlcNAc...) Potential
Glycosylation1911N-linked (GlcNAc...) Potential
Glycosylation4451N-linked (GlcNAc...) Potential
Glycosylation7021N-linked (GlcNAc...) Potential
Glycosylation7171N-linked (GlcNAc...) Potential
Glycosylation7281N-linked (GlcNAc...) Potential
Glycosylation8091N-linked (GlcNAc...) Potential
Glycosylation8701N-linked (GlcNAc...) Potential
Glycosylation10621N-linked (GlcNAc...) Potential
Glycosylation14571N-linked (GlcNAc...) Potential
Glycosylation15431N-linked (GlcNAc...) Potential
Glycosylation15731N-linked (GlcNAc...) Potential
Glycosylation17641N-linked (GlcNAc...) Potential
Glycosylation17821N-linked (GlcNAc...) Potential
Glycosylation18531N-linked (GlcNAc...) Potential
Disulfide bond381 ↔ 462 By similarity
Disulfide bond419 ↔ 446 By similarity
Disulfide bond568 ↔ 605 By similarity
Disulfide bond572 ↔ 610 By similarity
Disulfide bond583 ↔ 595 By similarity

Natural variations

Alternative sequence683 – 69311THDICVQGQCM → SYNIDCNCVLK in isoform 2.
Alternative sequence1430 – 150475CSASC…YCRLK → EDLKVKLLPQRTIILWELMK NIFCHGKHSHMYLINVVTDH LLYPRHCDPETIETYFLSLW SLQFTWGDLKYYKNSL in isoform 2.
Alternative sequence1505 – 1911407Missing in isoform 2.

Experimental info

Sequence conflict1521T → V in CAD56159 and CAD56160. Ref.2
Sequence conflict3601E → Y in CAD56159 and CAD56160. Ref.2
Sequence conflict3711T → M in CAD56159 and CAD56160. Ref.2
Sequence conflict4561D → E in CAD56159 and CAD56160. Ref.2
Sequence conflict6481I → V in CAD56159 and CAD56160. Ref.2
Sequence conflict792 – 7932Missing in CAD56159 and CAD56160. Ref.2
Sequence conflict818 – 8214LILQ → ILIE in CAD56159 and CAD56160. Ref.2
Sequence conflict908 – 9136GMLLAK → WHVIG in CAD56159. Ref.2
Sequence conflict13161S → Q in CAD56159 and CAD56160. Ref.2
Sequence conflict13281T → R in CAD56159 and CAD56160. Ref.2
Sequence conflict18171T → A in CAD56159. Ref.2
Sequence conflict18821E → Q in CAD56159. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 4, 2003. Version 1.
Checksum: CF592E220D32B250

FASTA1,911214,656
        10         20         30         40         50         60 
MWVAKWLTGL LYHLSLFITR SWEVDFHPRQ EALVRTLTSY EVVIPERVNE FGEVFPQSHH 

        70         80         90        100        110        120 
FSRQKRSSEA LEPMPFRTHY RFTAYGQLFQ LNLTADASFL AAGYTEVHLG TPERGAWESD 

       130        140        150        160        170        180 
AGPSDLRHCF YRGQVNSQED YKAVVSLCGG LTGTFKGQNG EYFLEPIMKA DGNEYEDGHN 

       190        200        210        220        230        240 
KPHLIYRQDL NNSFLQTLKY CSVSESQIKE TSLPFHTYSN MNEDLNVMKE RVLGHTSKNV 

       250        260        270        280        290        300 
PLKDERRHSR KKRLISYPRY IEIMVTADAK VVSAHGSNLQ NYILTLMSIV ATIYKDPSIG 

       310        320        330        340        350        360 
NLIHIVVVKL VMIHREEEGP VINFDGATTL KNFCSWQQTQ NDLDDVHPSH HDTAVLITRE 

       370        380        390        400        410        420 
DICSSKEKCN TLGLSYLGTI CDPLQSCFIN EEKGLISAFT IAHELGHTLG VQHDDNPRCK 

       430        440        450        460        470        480 
EMKVTKYHVM APALSFHMSP WSWSNCSRKY VTEFLDTGYG ECLLDKPDEE IYNLPSELPG 

       490        500        510        520        530        540 
SRYDGNKQCE LAFGPGSQMC PHINICMHLW CTSTEKLHKG CFTQHVPPAD GTDCGPGMHC 

       550        560        570        580        590        600 
RHGLCVNKET ETRPVNGEWG PWEPYSSCSR TCGGGIESAT RRCNRPEPRN GGNYCVGRRM 

       610        620        630        640        650        660 
KFRSCNTDSC PKGTQDFREK QCSDFNGKHL DISGIPSNVR WLPRYSGIGT KDRCKLYCQV 

       670        680        690        700        710        720 
AGTNYFYLLK DMVEDGTPCG TETHDICVQG QCMAAGCDHV LNSSAKIDKC GVCGGDNSSC 

       730        740        750        760        770        780 
KTITGVFNSS HYGYNVVVKI PAGATNVDIR QYSYSGQPDD SYLALSDAEG NFLFNGNFLL 

       790        800        810        820        830        840 
STSKKEINVQ GTRTVIEYSG SNNAVERINS TNRQEKELIL QVLCVGNLYN PDVHYSFNIP 

       850        860        870        880        890        900 
LEERSDMFTW DPYGPWEGCT KMCQGLQRRN ITCIHKSDHS VVSDKECDHL PLPSFVTQSC 

       910        920        930        940        950        960 
NTDCELRGML LAKKSECSSQ CGQGYRTLDI HCMKYSIHEG QTVQVDDHYC GDQLKPPTQE 

       970        980        990       1000       1010       1020 
LCHGNCVFTR WHYSEWSQCS RSCGGGERSR ESYCMNNFGH RLADNECQEL SRVTRENCNE 

      1030       1040       1050       1060       1070       1080 
FSCPSWAASE WSECLVTCGK GTKQRQVWCQ LNVDHLSDGF CNSSTKPESL SPCELHTCAS 

      1090       1100       1110       1120       1130       1140 
WQVGPWGPCT TTCGHGYQMR DVKCVNELAS AVLEDTECHE ASRPSDRQSC VLTPCSFISK 

      1150       1160       1170       1180       1190       1200 
LETALLPTVL IKKMAQWRHG SWTPCSVSCG RGTQARYVSC RDALDRIADE SYCAHLPRPA 

      1210       1220       1230       1240       1250       1260 
EIWDCFTPCG EWQAGDWSPC SASCGHGKTT RQVLCMNYHQ PIDENYCDPE VRPLMEQECS 

      1270       1280       1290       1300       1310       1320 
LAACPPAHSH FPSSPVQPSY YLSTNLPLTQ KLEDNENQVV HPSVRGNQWR TGPWGSCSSS 

      1330       1340       1350       1360       1370       1380 
CSGGLQHTAV VCQDENGQSA SYCDAASKPP ELQQCGPGPC PQWNYGNWGE CSQTCGGGIK 

      1390       1400       1410       1420       1430       1440 
SRLVICQFPN GQILEDHNCE IVNKPPSVIQ CHMHACPADV SWHQEPWTSC SASCGKGRKY 

      1450       1460       1470       1480       1490       1500 
REVFCIDQFQ RKLEDTNCSQ VQKPPTHKAC RSVRCPSWKA NSWNECSVTC GSGVQQRDVY 

      1510       1520       1530       1540       1550       1560 
CRLKGVGQVV EEMCDQSTRP CSQRRCWSQD CVQHKGMERG RLNCSTSCER KDSHQRMECT 

      1570       1580       1590       1600       1610       1620 
DNQIRQVNEI VYNSSTISLT SKNCRNPPCN YIVVTADSSQ CANNCGFSYR QRITYCTEIP 

      1630       1640       1650       1660       1670       1680 
STKKHKLHRL RPIVYQECPV VPSSQVYQCI NSCLHLATWK VGKWSKCSVT CGIGIMKRQV 

      1690       1700       1710       1720       1730       1740 
KCITKHGLSS DLCLNHLKPG AQKKCYANDC KSFTTCKEIQ VKNHIRKDGD YYLNIKGRII 

      1750       1760       1770       1780       1790       1800 
KIYCADMYLE NPKEYLTLVQ GEENFSEVYG FRLKNPYQCP FNGSRREDCE CDNGHLAAGY 

      1810       1820       1830       1840       1850       1860 
TVFSKIRIDL TSMQIKTTDL LFSKTIFGNA VPFATAGDCY SAFRCPQGQF SINLSGTGMK 

      1870       1880       1890       1900       1910 
ISSTAKWLTQ GSYTSVSIRR SEDGTRFFGK CGGYCGKCLP HMTTGLPIQV I 

« Hide

Isoform 2 [UniParc].

Checksum: CB4E32CA7FEC5E31
Show »

1,505169,441

References

[1]"Characterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1."
Somerville R.P., Longpre J.-M., Jungers K.A., Engle J.M., Ross M., Evanko S., Wight T.N., Leduc R., Apte S.S.
J. Biol. Chem. 278:9503-9513(2003) [PubMed: 12514189] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Identification and characterization of ADAMTS-20 defines a novel subfamily of metalloproteinases-disintegrins with multiple thrombospondin-1 repeats and a unique GON domain."
Llamazares M., Cal S., Quesada V., Lopez-Otin C.
J. Biol. Chem. 278:13382-13389(2003) [PubMed: 12562771] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Liver.

Cross-references

Sequence databases

AF488804 mRNA. Translation: AAO15766.1.
AJ515153 mRNA. Translation: CAD56159.3.
AJ515154 mRNA. Translation: CAD56160.2.
RefSeqNP_079279.3.
UniGeneHs.287554

3D structure databases

HSSPHSSP built from PDB template 1LSL based on UniProtKB P07996.
ModBaseSearch...

Protein family/group databases

MEROPSM12.246.

Genome annotation databases

EnsemblENSG00000173157. Homo sapiens. [Contig view]
GeneID80070.
KEGGhsa:80070.

Organism-specific databases

H-InvDBHIX0010556.
HGNCHGNC:17178. ADAMTS20.
MIM611681. gene.
PharmGKBPA134901626.
GenAtlasSearch...
GeneCardsSearch...
GeneLynxSearch...

Phylogenomic databases

HOVERGENP59510.

Gene expression databases

ArrayExpressP59510.
CleanExHS_ADAMTS20.
GermOnlineENSG00000173157. Homo sapiens.

Family and domain databases

InterProIPR010294. ADAM_spacer1.
IPR001762. Blood-coag_inhib_Disintegrin.
IPR012314. Pept_M12B_GON-ADAMTSs.
IPR006025. Pept_M_Zn_BS.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. TSP1.
[Graphical view]
PfamPF05986. ADAM_spacer1. 1 hit.
PF08685. GON. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 10 hits.
[Graphical view]
PRINTS